Alcohol dehydrogenase (ADH) (ADH)

Alcohol dehydrogenases (ADHs) are a group of zinc-containing enzymes that facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of NAD+ to NADH (StatPearls, 2023). In humans, these enzymes are categorized into seven distinct classes, with Class I isoenzymes (ADH1A, ADH1B, and ADH1C) being primarily responsible for the oxidation of ethanol in the liver (UniProt, 2024). Beyond ethanol metabolism, ADHs play a critical role in the processing of retinol into retinaldehyde, which is essential for vision and cellular differentiation (PubMed, 2021). They also serve a protective function by detoxifying formaldehyde and other reactive aldehydes produced during metabolic processes (NIH, 2022). Clinically, ADH is the primary target for treating toxic alcohol ingestions, such as methanol or ethylene glycol poisoning, where the inhibitor fomepizole is used to block the formation of toxic metabolites (PubChem, 2023). Genetic polymorphisms in ADH genes, particularly the ADH1B*2 allele, significantly influence an individual's rate of alcohol metabolism and their risk for developing alcohol use disorders (Wikipedia, 2024). These enzymes are also implicated in the pathogenesis of certain cancers, as the byproduct acetaldehyde is a known carcinogen (PubMed, 2020). Overall, ADH isoenzymes are central to both physiological nutrient metabolism and the pharmacological management of acute chemical toxicities.

Other names

Alcohol:NAD+ oxidoreductaseADH familyClass I alcohol dehydrogenaseClass II alcohol dehydrogenaseClass III alcohol dehydrogenaseClass IV alcohol dehydrogenaseAldehyde reductaseRetinol dehydrogenase

Competitive inhibition of the enzyme's active site, specifically the zinc-binding catalytic center, to prevent the oxidation of alcohols into toxic aldehydes.